Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study

Autores
Kranich, Anja; Naumann, Hendrik; Molina Heredia, Fernando P.; Moore, H. Justin; Lee, T. Randall; Lecomte, Sophie; Nuñez de la Rosa, Eduardo Miguel; Hildebrandt, Peter; Murgida, Daniel Horacio
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The electron shuttle heme protein Cyt-c6 from the photosynthetic cyanobacterium Nostoc sp. PCC 7119 was immobilized on nanostructured Ag electrodes coated with SAMs that mimic different possible interactions with its natural reaction partner PSI. The structure, redox potential, and electron-transfer dynamics of the SAM-Cyt-c6 complexes were investigated by TR-SERR spectroelectrochemistry. It is shown that the heterogeneous electron-transfer process is gated both in electrostatic and hydrophobic-hydrophilic complexes. At long tunneling distances, the reaction rate is controlled by the tunneling probability, while at shorter distances or higher driving forces, protein dynamics becomes the rate-limiting event.
Fil: Kranich, Anja. Technische Universität Berlin; Alemania
Fil: Naumann, Hendrik. Technische Universität Berlin; Alemania
Fil: Molina Heredia, Fernando P.. Universidad de Sevilla; España. Consejo Superior de Investigaciones Científicas; España
Fil: Moore, H. Justin. University Of Houston; Estados Unidos
Fil: Lee, T. Randall. University Of Houston; Estados Unidos
Fil: Lecomte, Sophie. Universite de Bordeaux; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Nuñez de la Rosa, Eduardo Miguel. Universidad de Sevilla; España. Consejo Superior de Investigaciones Científicas; España
Fil: Hildebrandt, Peter. Technische Universität Berlin; Alemania
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Materia
Citocromos
Redox Proteins
Raman
Protein Dynamics
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/75275
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR studyKranich, AnjaNaumann, HendrikMolina Heredia, Fernando P.Moore, H. JustinLee, T. RandallLecomte, SophieNuñez de la Rosa, Eduardo MiguelHildebrandt, PeterMurgida, Daniel HoracioCitocromosRedox ProteinsRamanProtein Dynamicshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The electron shuttle heme protein Cyt-c6 from the photosynthetic cyanobacterium Nostoc sp. PCC 7119 was immobilized on nanostructured Ag electrodes coated with SAMs that mimic different possible interactions with its natural reaction partner PSI. The structure, redox potential, and electron-transfer dynamics of the SAM-Cyt-c6 complexes were investigated by TR-SERR spectroelectrochemistry. It is shown that the heterogeneous electron-transfer process is gated both in electrostatic and hydrophobic-hydrophilic complexes. At long tunneling distances, the reaction rate is controlled by the tunneling probability, while at shorter distances or higher driving forces, protein dynamics becomes the rate-limiting event.Fil: Kranich, Anja. Technische Universität Berlin; AlemaniaFil: Naumann, Hendrik. Technische Universität Berlin; AlemaniaFil: Molina Heredia, Fernando P.. Universidad de Sevilla; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Moore, H. Justin. University Of Houston; Estados UnidosFil: Lee, T. Randall. University Of Houston; Estados UnidosFil: Lecomte, Sophie. Universite de Bordeaux; Francia. Centre National de la Recherche Scientifique; FranciaFil: Nuñez de la Rosa, Eduardo Miguel. Universidad de Sevilla; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Hildebrandt, Peter. Technische Universität Berlin; AlemaniaFil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaRoyal Society of Chemistry2009-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/75275Kranich, Anja; Naumann, Hendrik; Molina Heredia, Fernando P.; Moore, H. Justin; Lee, T. Randall; et al.; Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 11; 34; 12-2009; 7390-73971463-9076CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1039/b904434einfo:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2009/CP/b904434einfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:19:41Zoai:ri.conicet.gov.ar:11336/75275instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:19:41.393CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
title Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
spellingShingle Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
Kranich, Anja
Citocromos
Redox Proteins
Raman
Protein Dynamics
title_short Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
title_full Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
title_fullStr Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
title_full_unstemmed Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
title_sort Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study
dc.creator.none.fl_str_mv Kranich, Anja
Naumann, Hendrik
Molina Heredia, Fernando P.
Moore, H. Justin
Lee, T. Randall
Lecomte, Sophie
Nuñez de la Rosa, Eduardo Miguel
Hildebrandt, Peter
Murgida, Daniel Horacio
author Kranich, Anja
author_facet Kranich, Anja
Naumann, Hendrik
Molina Heredia, Fernando P.
Moore, H. Justin
Lee, T. Randall
Lecomte, Sophie
Nuñez de la Rosa, Eduardo Miguel
Hildebrandt, Peter
Murgida, Daniel Horacio
author_role author
author2 Naumann, Hendrik
Molina Heredia, Fernando P.
Moore, H. Justin
Lee, T. Randall
Lecomte, Sophie
Nuñez de la Rosa, Eduardo Miguel
Hildebrandt, Peter
Murgida, Daniel Horacio
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Citocromos
Redox Proteins
Raman
Protein Dynamics
topic Citocromos
Redox Proteins
Raman
Protein Dynamics
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The electron shuttle heme protein Cyt-c6 from the photosynthetic cyanobacterium Nostoc sp. PCC 7119 was immobilized on nanostructured Ag electrodes coated with SAMs that mimic different possible interactions with its natural reaction partner PSI. The structure, redox potential, and electron-transfer dynamics of the SAM-Cyt-c6 complexes were investigated by TR-SERR spectroelectrochemistry. It is shown that the heterogeneous electron-transfer process is gated both in electrostatic and hydrophobic-hydrophilic complexes. At long tunneling distances, the reaction rate is controlled by the tunneling probability, while at shorter distances or higher driving forces, protein dynamics becomes the rate-limiting event.
Fil: Kranich, Anja. Technische Universität Berlin; Alemania
Fil: Naumann, Hendrik. Technische Universität Berlin; Alemania
Fil: Molina Heredia, Fernando P.. Universidad de Sevilla; España. Consejo Superior de Investigaciones Científicas; España
Fil: Moore, H. Justin. University Of Houston; Estados Unidos
Fil: Lee, T. Randall. University Of Houston; Estados Unidos
Fil: Lecomte, Sophie. Universite de Bordeaux; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Nuñez de la Rosa, Eduardo Miguel. Universidad de Sevilla; España. Consejo Superior de Investigaciones Científicas; España
Fil: Hildebrandt, Peter. Technische Universität Berlin; Alemania
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
description The electron shuttle heme protein Cyt-c6 from the photosynthetic cyanobacterium Nostoc sp. PCC 7119 was immobilized on nanostructured Ag electrodes coated with SAMs that mimic different possible interactions with its natural reaction partner PSI. The structure, redox potential, and electron-transfer dynamics of the SAM-Cyt-c6 complexes were investigated by TR-SERR spectroelectrochemistry. It is shown that the heterogeneous electron-transfer process is gated both in electrostatic and hydrophobic-hydrophilic complexes. At long tunneling distances, the reaction rate is controlled by the tunneling probability, while at shorter distances or higher driving forces, protein dynamics becomes the rate-limiting event.
publishDate 2009
dc.date.none.fl_str_mv 2009-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/75275
Kranich, Anja; Naumann, Hendrik; Molina Heredia, Fernando P.; Moore, H. Justin; Lee, T. Randall; et al.; Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 11; 34; 12-2009; 7390-7397
1463-9076
CONICET Digital
CONICET
url http://hdl.handle.net/11336/75275
identifier_str_mv Kranich, Anja; Naumann, Hendrik; Molina Heredia, Fernando P.; Moore, H. Justin; Lee, T. Randall; et al.; Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 11; 34; 12-2009; 7390-7397
1463-9076
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1039/b904434e
info:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2009/CP/b904434e
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842981075989561344
score 12.48226

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